Agilent 1100 series lc msd trap xct ultra mass spectrometer

Manufactured by Agilent Technologies

Sourced in United States

The Agilent 1100 series LC/MSD Trap XCT Ultra mass spectrometer is a high-performance liquid chromatography-mass spectrometry (LC/MS) system designed for chemical analysis. It combines liquid chromatography with an ion trap mass spectrometer to provide reliable and sensitive detection of a wide range of analytes. The system is capable of accurate mass measurement and can be used for a variety of applications, including drug discovery, environmental analysis, and food testing.

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Lab products found in correlation

Chemstation 1200 series, by Agilent Technologies (3 mentions)

Close spelling variants of this product

Agilent 1100 Series LC/MSD Trap mass spectrometer Agilent 1100 Series LC-MSD-Trap-XCT LC/MSD trap XCT mass spectrometer Agilent 1100 Series LC/MSD Trap 1100 series LC/MSD (XCT) LC/MSD Trap XCT Ultra 1100 Series LC/MSD Trap 1100 Series LC/MSD spectrometer LC-MSD 1100 series Agilent 1100 Series LC

4 protocols using agilent 1100 series lc msd trap xct ultra mass spectrometer

Solid-Phase Peptide Synthesis and Characterization

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Peptides were synthesized by solid phase method using amino acid derivatives with 9-fluorenylmethyloxycarbonyl (Fmoc) protected α-amino groups (Novabiochem). The procedure was performed as described elsewhere (Kuznetsova et al. 2018) (link) ). In more details, the peptides are shown in Table 1. Further steps of synthesis were also performed as described earlier (C. A. Hood et al. 2008) (link).
For quality control of the synthesis, LC-MS analysis was done using a chromatographic Agilent ChemStation 1200 series connected to an Agilent 1100 series LC/MSD Trap XCT Ultra mass spectrometer (Agilent, USA). Since some peptides contained methionines, the quality control also included manual inspection of the MS and MS/MS spectra for possible presence of the peaks produced by oxidized compounds. No such peaks were found in our case.
Absolute concentrations of synthesized peptides were determined using conventional amino acid analysis with their orthophthalic derivatives according to standard amino acid samples.

Levitsky L.I., Ivanov M.V., Goncharov A.O., Kliuchnikova A.A., Bubis J.A., Lobas A.A., Solovyeva E.M., Pyatnitskiy M.A., Ovchinnikov R.K., Kukharsky M.S., Farafonova T.E., Novikova S.E., Zgoda V.G., Tarasova I.A., Gorshkov M.V, & Moshkovskii S.A. (2023). Massive Proteogenomic Reanalysis of Publicly Available Proteomic Datasets of Human Tissues in Search for Protein Recoding via Adenosine-to-Inosine RNA Editing. Journal of proteome research, 22(6).

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Robust Peptide Synthesis and Characterization

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Peptides were synthesized by solid phase method using amino acid derivatives with 9-fluorenyl methyloxy carbonyl (Fmoc) protected α-amino groups (Novabiochem). The procedure was performed as described previously [16] (link). Stable isotope containing leucine (Fmoc-Leu-OH- was used for synthesis of peptides of CG4587 (LVTTVSTPVFDR h and LVTTVSTPVFDGR h ) and Atx2 (GVGPAPSANASADSSSR h ). Further steps of synthesis were also performed as described earlier [67] (link).
For quality control of the synthesis, LC-MS analysis was done using a chromatographic Agilent ChemStation 1200 series connected to an Agilent 1100 series LC/MSD Trap XCT Ultra mass spectrometer (Agilent, USA). Since some peptides contained methionines, the quality control also included manual inspection of the MS and MS/MS spectra for possible presence of the peaks produced by oxidized compounds. No such peaks were found in our case.
Absolute concentrations of synthesized peptides were determined using conventional amino acid analysis with their orthophthalic derivatives according to standard amino acid samples.

Kliuchnikova A.A., Goncharov A.O., Levitsky L.I., Pyatnitskiy M.A., Новикова С., Kuznetsova K.G., Ivanov M.V., Ilina I.Y., Farafonova T., Zgoda V.G., Gorshkov M.V., & Moshkovskii S.A. (2020). Proteome-Wide Analysis of ADAR-mediated Messenger RNA Editing During Fruit Fly Ontogeny.

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Robust Peptide Synthesis and Characterization

Check if the same lab product or an alternative is used in the 5 most similar protocols

Peptides were synthesized by solid phase method using amino acid derivatives with 9-fluorenyl methyloxy carbonyl (Fmoc) protected α-amino groups (Novabiochem). The procedure was performed as described previously [16] (link). Stable isotope containing leucine (Fmoc-Leu-OH- was used for synthesis of peptides of CG4587 (LVTTVSTPVFDR h and LVTTVSTPVFDGR h ) and Atx2 (GVGPAPSANASADSSSR h ). Further steps of synthesis were also performed as described earlier [67] (link).
For quality control of the synthesis, LC-MS analysis was done using a chromatographic Agilent ChemStation 1200 series connected to an Agilent 1100 series LC/MSD Trap XCT Ultra mass spectrometer (Agilent, USA). Since some peptides contained methionines, the quality control also included manual inspection of the MS and MS/MS spectra for possible presence of the peaks produced by oxidized compounds. No such peaks were found in our case.
Absolute concentrations of synthesized peptides were determined using conventional amino acid analysis with their orthophthalic derivatives according to standard amino acid samples.

Kliuchnikova A.A., Goncharov A.O., Levitsky L.I., Pyatnitskiy M.A., Novikova S.E., Kuznetsova K.G., Ivanov M.V., Ilina I.Y., Farafonova T.E., Zgoda V.G., Gorshkov M.V, & Moshkovskii S.A. (2020). Proteome-Wide Analysis of ADAR-Mediated Messenger RNA Editing during Fruit Fly Ontogeny. Journal of proteome research, 19(10).

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Solid-Phase Synthesis of Stable Isotope-Labeled Peptides

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Peptides were synthesised by solid phase method using amino acid derivatives with 9-fluorenyl methyloxy carbonyl (Fmoc) protected α-amino groups (Novabiochem).
The procedure was performed as described elsewhere 35 . Stable isotope-containing leucine (Fmoc-Leu-OH-13 C6, 15 N, Cambridge Isotope Laboratories) was applied for labeling 11-plex peptides from cpx protein (NQMETQVNEL h K and NQIETQVNEL h K).
A resin with attached stable isotope-labeled lysine (L-Lys (Boc) ( 13 Further steps of synthesis were also preceded as described 35 .
For synthesis quality control, a simple LC-MS analysis was held using a chromatographic Agilent ChemStation 1200 series connected to an Agilent 1100 series LC/MSD Trap XCT Ultra mass spectrometer (Agilent, USA). Since our peptides contained methionine residues, the quality control also included manual inspection of the MS and MS/MS spectra for possible presence of the peaks produced by oxidized compounds. No such peaks were found in our case.
Concentrations of synthesised peptides were determined using conventional amino acid analysis with their orthophtalic derivatives according to standard amino acid samples.

Kuznetsova K.G., Kliuchnikova A.A., Ilina I.U., Chernobrovkin A.L., Novikova S.E., Farafonova T.E., Karpov D.S., Ivanov M.V., Goncharov A.O., Ilgisonis E.V., Voronko O.E., Nasaev S.S., Zgoda V.G., Zubarev R.A., Gorshkov M.V, & Moshkovskii S.A. (2018). Proteogenomics of Adenosine-to-Inosine RNA Editing in the Fruit Fly. Journal of proteome research, 17(11).

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